Rigor mortis - UNIRIO

Profa. dra. Édira Castello Branco de Andrade Gonçalves

http://www.unirio.br/analisedealimentos

Rigor mortis


http://faculty.southwest.tn.edu/rburkett/gb%201%20cell%20resp.htm

RESPIRATION


http://ib.bioninja.com.au/standard-level/topic-2-molecular-biology/28-cell-respiration/anaerobic-respiration.html

RESPIRATION


FERMENTATION

Myosin

http://physiologyonline.physiology.org/content/15/1/26

https://www.slideshare.net/suknamgoong/cell-bio7

MUSCLE CONTRACTION


MUSCLE CONTRACTION

higheredbcs.wiley.com

http://higheredbcs.wiley.com/legacy/college/tortora/0470565101/hearthis_ill/pap13e_ch10_illustr_audio_mp3_am/simulations/hear/contraction_cycle.html


Regnier & Cheng 2016


Rigor Mortis as a Function of Meat Chemistry and Time The timing of

the stages of rigor mortis varies between species. Poultry is often in rigor

within 1-2 hours, pork within 4 to 6 hours, beef and lamb within 7 to 15

hours after exsanguination.

http://qpc.adm.slu.se/6_Fundamentals_of_WHC/page_16.htm


Compound Color Name

-CN Red Cyanmetmyoglobin

-OH Brown Metmyoglobin

-SH Green Sulfmyoglobin

-H2O2 Green Choleglobin

Compound Color Name

:H2O Purple Reduced myoglobin

or deoxymyoglobin

:O2 Red Oxymyoglobin

:NO Cured pink Nitric oxide

myoglobin

:CO Red Carboxymyoglobin

Chemical state of myoglobin

(covalent bonds)

Chemical state of myoglobin

(ionic bonds)

http://meat.tamu.edu/ansc-307-honors/meat-color/


Four Categories of Pork Quality

RFN

Red, Firm, Non-exudative.

Minolta L* less than 50; pH

between 5.5 – 6.1

RSE

Red, Soft, Exudative.

Minolta L* less than 50; pH less

than 5.6

PSE

Pale, Soft, Exudative. Minolta L*

greater than 50; pH less than 5.5

DFD

Dark, Firm, Dry. Minolta L* less

than 38; pH greater than 6.1

http://www.thepigsite.com/articles/5341/pork-meat-quality-understanding-industry-

measurements-and-guidelines/


Water Holding Capacity (WHC) of Meat

http://qpc.adm.slu.se/6_Fundamentals_of_WHC/page_21.htm


Effect of seasonality and storage temperature on rigor mortis in the

adductor muscle of lion's paw scallop Nodipecten subnodosus

The effect of season and storage at three temperatures (0, 5 and 10 °C) was

evaluated on the main metabolites and parameters related to rigor mortis.

Adenosine 5′-triphosphate (ATP), lactic acid, octopine, pH and sarcomere length

in the adductor muscle of lion's paw scallop Nodipecten subnodosus were

determined. Seasonality influenced the initial values of ATP, octopine and pH, however, no effect was noticed during storage, since a similar effect for the three

temperatures evaluated in the four seasons was observed. A lower ATP

concentration was found during storage at 0 °C than that found in muscle stored

at 5 and 10 °C. According to the analyses of lactic acid, octopine and pH, the

muscle acidification during rigor mortis was independent of lactic acid production. The greater sarcomere lengths for all seasons were in agreement

with the highest ATP concentrations, corresponding to the samples stored at 5

and 10 °C. Therefore, according to the level of myofibrillar contraction, rigor

mortis was lower at 5 and 10 °C storage in the four seasons. Hence, it is

concluded that the seasonality did not show a significant impact on metabolite and parameter values related to rigor mortis during storage, and that 5 °C is the

best storage temperature for the adductor muscles during the initial stage

of rigor mortis and then reduce it to 0 °C, if it is focused to the fresh market.

Jiménez-Ruiz et al. 2013


ATP concentration in the

adductor muscle of lion's paw

scallop N.

subnodosus harvested at

distinct seasons and stored at different temperatures. a)

Spring, b) summer, c)

autumn, and d) winter.

Lactic acid concentration

in the adductor muscle of

lion's paw scallop N.

subnodosusharvested at

distinct seasons and stored at different

temperatures. a) Spring, b)

summer, c) autumn, and d)

winter.



pH values in the adductor

muscle of lion's paw

scallop N.

subnodosus harvested at

distinct seasons and stored at different temperatures. a)

Spring, b) summer, c)

autumn, and d) winter.

octopine is considered

as one of the possible

final metabolites of

anaerobic glycolysis

for certain invertebrates



Comparative profiling of sarcoplasmic phosphoproteins

in ovine muscle with different color stability

The phosphorylation of sarcoplasmic proteins in postmortem muscles was

investigated in relationship to color stability in the present study. Although no

difference was observed in the global phosphorylation level of sarcoplasmic

proteins, difference was determined in the phosphorylation levels of individual

protein bands from muscles with different color stability. Correlation analysis and liquid chromatography – tandem mass spectrometry (LC-MS/MS)

identification of phosphoproteins showed that most of the color stability-related

proteins were glycolytic enzymes. Interestingly, the phosphorylation level of

myoglobin was inversely related to meat color stability. As the phosphorylation

of myoglobin increased, color stability based on a∗ value decreased and metMb content increased. In summary, the study revealed that protein

phosphorylation might play a role in the regulation of meat color stability

probably by regulating glycolysis and the redox stability of myoglobin, which

might be affected by the phosphorylation of myoglobin.

Li et al. 2017


Gel-base analysis of

sarcoplasmic protein phosphorylation Li et al. 2017


Underlying connections between the redox system imbalance, protein oxidation

and impaired quality traits in pale, soft and exudative (PSE) poultry meat

The connections between the redox imbalance in post-mortem muscle, early protein

oxidation and the onset of pale, soft and exudative (PSE) condition in chicken breast

are studied. PSE was induced by incubation of post-mortem chicken carcasses at

37 °C for 200 min. PSE-induced muscle consistently had faster pH decline and

lower pH at 200 min (5.84 vs. 6.59) and 24 h (5.69 vs. 5.96), higher L∗ (54.4 vs. 57.3), and lower texture and water holding capacity (WHC) than normal meat. The

activities of catalase, glutathione peroxidase and superoxide dismutase were

significantly lower in PSE-induced samples than in the normal counterparts. PSE

was more susceptible to proteolysis and protein oxidation than normal meat during

succeeding chilled storage with more intense tryptophan and thiols depletion, higher protein carbonylation and more intense formation of protein cross-links. We provide

plausible explanations to support the role of protein oxidation in the impaired quality PSE chicken.

Carvalho et al. 2017


Evolution of pH in normal and

PSE-induced breast broiler meat during

24 h following slaughter.

Tryptophan (mg NATA/g protein) (A) and free

thiols (μmol thiols/mg sample) (B) depletion

during chilled storage of normal and PSE-induced

breast broiler meat.




Formation of oxidation products: protein carbonyls (nmol carbonyls/mg protein)

(A) TBA-RS (mg MDA/kg muscle) (B), Schiff bases (fluorescence intensity) (C) and

disulphide bonds (μmol thiols/mg sample) (D) during chilled storage at 4 °C of normal

and PSE-induced breast broiler meat.


Applications of high pressure to pre-rigor rabbit muscles

affect the water characteristics of myosin gels

Myosin was extracted immediately after high-pressure treatment (HP,

100–300 MPa for 15 or 180 s) to pre-rigor rabbit muscles (PRRMs) for

evaluating the influences of HP-treatment on gel properties, using

untreated muscles as Controls. Assessment of myosin yields, water-

holding capacity (WHC), water mobility and distribution demonstrated that HP modified myosin before its extraction. Myosin gels subjected to

HP at 100 MPa 180 s and 200 MPa 15 s had enhanced WHC

compared with Controls. Also, the highest proportion of immobile-water

was observed in myosin gels treated at 200 MPa for 15 s. HP-

treatment of PRRMs affected their physicochemical properties as evidenced by alterations in tertiary, secondary conformations and

rheological properties during subsequent heating. These modifications

appear to induce various degrees of exposure of hydrophobic and

sulfhydryl groups, resulting in different gelation rates. These alterations

partly explain the various gel qualities obtained and indicate the potential of HP for pre-rigor muscles.

Xue et al. 2017


Yields of myosin extracted from PRRMs

following various HP

treatments. Note: Means with different

superscripts (a–e)

Water holding capacity (WHC) of

myosin gels. Xue et al. 2017


Changes in the hydrophobicity of various myosin

samples when heated from 25 to 85 °C.

The Surface hydrophobicity (H0) is an important

indicator of protein

conformation changes,

and the exposure of buried hydrophobic

residues has been

considered as a

prerequisite for the aggregation of myosin

Xue et al. 2017


Changes in the sulfhydryl contents of of various

myosin samples when heated from 25-85°C

The tertiary changes of

myosin are mainly

related to those based

on non-covalent

interactions and the breaking of some non-

covalent bonds which

are beneficial for the

exposure of buried

amino groups, such as hydrophobic groups

and sulfhydryl groups

Xue et al. 2017


Storage modulus (G′) of various myosin solutions

The gelling process of meat

proteins usually occurs in three

stages: 1) an initial increase in

G′, ascribed to the denaturation

and aggregation of the head and hinge components of

myosin; 2) followed by a

reduction of G′ induced by the

denaturation of myosin tails,

which may disrupt the weak gel network, leading to the

enhancement of fluidity; 3)

finally, where the denatured

myosin is aggregated and

bound to form an organized gel network.


Effect of sodium alginate with three molecular weight forms

on the water holding capacity of chicken breast myosin gel

The effect of 0.1–0.5% (w/w) sodium-alginate (SA) with three

molecular-weights (2660, 3890 and 4640 kDa) on the water-holding

capacity (WHC) of chicken-breast myosin gels was investigated. The

results showed that 0.1–0.5% SA of three molecular-weights

increased the WHC of myosin-SA gels, and the heavier SA induced a higher WHC. Electrostatic-interactions and hydrogen-bonding

contributed to the intermolecular aggregation in the myosin-SA system

and enhanced its intermolecular interactions by overcoming the steric

hindrance effect of SA with heavier molecules. This aggregation

induced the increased turbidity, transition temperature and the decreased surface hydrophobicity of myosin-SA solutions and the

formation of an inhomogeneous network with large cavities for

entrapping water. The combined effects of stronger intermolecular

interactions and the network induced a higher WHC of the gel with

heavier SA. It is interesting to understand the gelling mechanism for the protein-polysaccharide system and to efficiently select SA for

developing low-fat meat products in industry.

Yao et al. 2018


Effects of L-SA, M-SA and H-SA on

the WHC of myosin gels

Effects of L-SA, M-SA and H-SA

on the turbidity (A) and the surface

hydrophobicity (B) of myosin gels.

Yao et al. 2018


WHC of myosin with 0.3% SA (A) and 0.5% SA

(B) gels as affected by chemical reagents

Treatment Tpeak1 (°C) Tpeak2 (°C)

Myosin 53.87 ± 0.39a 65.14 ± 0.30a

Myosin + 0.5% L-SA 54.54 ± 0.47a 65.85 ± 0.40ab

Myosin + 0.5% M-SA 54.14 ± 0.22a 66.87 ± 0.23b

Myosin + 0.5% H-SA 54.83 ± 0.36a 67.31 ± 0.00c

Transition temperature (Tpeak) of myosin,

myosin + L-SA, myosin + M-SA and

myosin + H-SA.*

Yao et al. 2018

http://www-sciencedirect-com.ez39.periodicos.capes.gov.br/science/article/pii/S030881461731172X?via%3Dihub

Carvalho, R.H. et al., 2017. Underlying connections between the redox system imbalance, protein oxidation and impaired qualit y traits in pale, soft

and exudative (PSE) poultry meat. Food Chemistry, 215, pp.129–137. Available at: http://ac-els-cdn-

com.ez39.periodicos.capes.gov.br/S0308814616312158/1-s2.0-S0308814616312158-main.pdf?_tid=179fa19c-8100-11e7-b1a1-

00000aab0f27&acdnat=1502722485_0a16a67a574f320f9b3a5d988ac24c4c [Acedido Agosto 14, 2017].

Damodaran, S., Parkin, K.L. & Fennema, O.R., 2010. Quimica de Alimentos de Fennema 4.a ed. Artmed, ed., Porto Alegre.

Édira Castelo Branco de Andrade, 2015. Análise de alimentos - uma visão química da Nutrição Varela, ed., São Paulo.

Ertbjerg, P. & Puolanne, E., 2017. Muscle structure, sarcomere length and influences on meat quality: A review. Meat Science. Available at:

www.elsevier.com/locate/meatsci [Acedido Agosto 12, 2017].

Jiménez-Ruiz, E.I. et al., 2013. Effect of seasonality and storage temperature on rigor mortis in the adductor muscle of lion’s paw scallop Nodipecten

subnodosus. Aquaculture, 388–391(1), pp.35–41. Available at: http://ac-els-cdn-com.ez1.periodicos.capes.gov.br/S0044848613000100/1-s2.0-

S0044848613000100-main.pdf?_tid=7449c7ae-7f1d-11e7-9029-00000aacb362&acdnat=1502515194_48a39a774413a426b1a9234c1e1ac9fd

[Acedido Agosto 12, 2017].

Li, M. et al., 2017. Comparative profiling of sarcoplasmic phosphoproteins in ovine muscle with different color stability. Available at: http://ac-els-

cdn-com.ez1.periodicos.capes.gov.br/S0308814617312505/1-s2.0-S0308814617312505-main.pdf?_tid=d3d91754-7f1f-11e7-be88-

00000aacb35f&acdnat=1502516213_fa74b09f994691a3aea7deb562850619 [Acedido Agosto 12, 2017].

Regnier, M. & Cheng, Y., 2016. Finally, We Can Relax: A New Generation of Muscle Models that Incorporate Sarcomere Compliance . Biophysical

Journal, 110(3), pp.521–522.

Xue, S. et al., 2017. Applications of high pressure to pre-rigor rabbit muscles affect the functional properties associated with heat-induced gelation.

Meat Science, 129, pp.176–184. Available at: www.elsevier.com/locate/foodchem [Acedido Agosto 14, 2017].

Yao, J. et al., 2018. Effect of sodium alginate with three molecular weight forms on the water holding capacity of chicken breast myosin gel. , 239,

pp.1134–1142. Available at: http://ac-els-cdn-com.ez39.periodicos.capes.gov.br/S030881461731172X/1-s2.0-S030881461731172X-

main.pdf?_tid=c988e93a-8106-11e7-bd8e-00000aacb362&acdnat=1502725361_67348016d5d4cb463dc2bd773ed71a98 [Acedido Agosto 14,

2017].

Yildiz, F., 2010. Advances in food biochemistry, CRC Press.

References

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